Document Type
Article
Version Deposited
Published Version
Publication Date
11-14-2023
Publication Title
Antibiotics (Basel)
DOI
10.3390/antibiotics12111624
Abstract
Antimicrobial resistance continues to be a major threat to world health, with the continued emergence of resistant bacterial strains. Antimicrobial peptides have emerged as an attractive option for the development of novel antimicrobial compounds in part due to their ubiquity in nature and the general lack of resistance development to this class of molecules. In this work, we analyzed the antimicrobial peptide C18G and several truncated forms for efficacy and the underlying mechanistic effects of the sequence truncation. The peptides were screened for antimicrobial efficacy against several standard laboratory strains, and further analyzed using fluorescence spectroscopy to evaluate binding to model lipid membranes and bilayer disruption. The results show a clear correlation between the length of the peptide and the antimicrobial efficacy. Furthermore, there is a correlation between peptide length and the hydrophobic thickness of the bilayer, indicating that hydrophobic mismatch is likely a contributing factor to the loss of efficacy in shorter peptides.
Recommended Citation
Meier, S.; Ridgway, Z.M.; Picciano, A.L.; Caputo, G.A. Impacts of Hydrophobic Mismatch on Antimicrobial Peptide Efficacy and Bilayer Permeabilization. Antibiotics 2023, 12, 1624. https://doi.org/10.3390/antibiotics12111624
Creative Commons License
This work is licensed under a Creative Commons Attribution 4.0 International License.
Comments
Copyright: © 2023 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license.